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<p>Motility promotes the complex life cycle and infectious capabilities of <i>Vibrio cholerae</i> and is driven by rotation of a single polar flagellum. The flagellar filament comprises four flagellin proteins (FlaA–D) and is covered by a membranous sheath continuous with the outer membrane. Here we combine in situ cryo-electron microscopy single-particle analysis, fluorescence microscopy and molecular genetics to determine 2.92–3.43 Å structures of the sheathed flagellar filament from intact bacteria. Our data reveal the spatial arrangement of FlaA–D, showing that FlaA localizes at the cell pole and functions as a template for filament assembly involving multiple flagellins. Unlike unsheathed flagellar filaments, the sheathed filament from <i>V. cholerae</i> possesses a highly conserved core but a smooth, hydrophilic surface adjacent to the membranous sheath. A tiny conformational change at the single flagellin level results in a supercoiled filament and curved membranous sheath, supporting a model wherein the filament rotates separately from the sheath, enabling the distinct motility of <i>V. cholerae</i>.</p>

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Structures of the sheathed flagellum reveal mechanisms of assembly and rotation in Vibrio cholerae

  • 期刊论文

  • 发表日期：

    2025年10月31日

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  • Wangbiao Guo,
  • Sarah Zhang,
  • Jin Hwan Park,
  • Venus Stanton,
  • Merrill Asp,
  • Helen Herrera,
  • Jung-Shen Benny Tai,
  • Jian Yue,
  • Jiaqi Wang,
  • Jiaqi Guo,
  • Rajeev Kumar,
  • Jack M. Botting,
  • Shenping Wu,
  • Jing Yan,
  • Karl E. Klose,
  • Fitnat H. Yildiz,
  • Jun Liu

摘要

Motility promotes the complex life cycle and infectious capabilities of Vibrio cholerae and is driven by rotation of a single polar flagellum. The flagellar filament comprises four flagellin proteins (FlaA–D) and is covered by a membranous sheath continuous with the outer membrane. Here we combine in situ cryo-electron microscopy single-particle analysis, fluorescence microscopy and molecular genetics to determine 2.92–3.43 Å structures of the sheathed flagellar filament from intact bacteria. Our data reveal the spatial arrangement of FlaA–D, showing that FlaA localizes at the cell pole and functions as a template for filament assembly involving multiple flagellins. Unlike unsheathed flagellar filaments, the sheathed filament from V. cholerae possesses a highly conserved core but a smooth, hydrophilic surface adjacent to the membranous sheath. A tiny conformational change at the single flagellin level results in a supercoiled filament and curved membranous sheath, supporting a model wherein the filament rotates separately from the sheath, enabling the distinct motility of V. cholerae.